C4695
CHAPSO
BioXtra
Synonym(s):
3-([3-Cholamidopropyl]dimethylammonio)-2-hydroxy-1-propanesulfonate
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About This Item
Empirical Formula (Hill Notation):
C32H58N2O8S
CAS Number:
Molecular Weight:
630.88
Beilstein/REAXYS Number:
5842642
MDL number:
UNSPSC Code:
12161900
PubChem Substance ID:
NACRES:
NA.25
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description
zwitterionic
Quality Level
product line
BioXtra
assay
≥98.0% (TLC)
form
powder
mol wt
micellar avg mol wt 7000
aggregation number
11
impurities
≤0.0005% Phosphorus (P)
≤0.1% Insoluble matter (in Ethanol)
ign. residue
≤0.1%
CMC
8 mM (20-25°C)
8 mM (micellar weight =9960)
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General description
Chapso is a zwitterionic detergent derived from Chaps by the addition of a functional hydroxyl group. It is a nondenaturing zwitterionic detergent with characteristics similar to CHAPS, although it is more soluble due to a more polar head group.
Application
A nondenaturing zwitterionic detergent with characteristics similar to CHAPS, although it is more soluble due to a more polar head group. Useful for the solubilization of integral membrane proteins.
Chapso has been used in a study to assess methods for high-throughput crystallization of membrane proteins. It has also been used in a study to investigate the effects of detergents on the structure of rhomboid proteases in a lipid environment.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
ppe
dust mask type N95 (US), Eyeshields, Gloves
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Incomplete Dialysis of Protein Samples Containing 3-[(3-Cholamidopropyl)dimethylammonio]-1-propanesulfonate May Lead to Erroneous Estimation of Histidine Content on Amino Acid Analysis
Nomura, K., et al.
Analytical Biochemistry, 290, 4-4 (2001)
Structure of Rhomboid Protease in a Lipid Environment
Vinothkumar, K., et al.
Journal of Molecular Biology, 407, 16-16 (2011)
Rachna Ujwal et al.
Methods (San Diego, Calif.), 55(4), 337-341 (2011-10-11)
Crystallization of membrane proteins remains a significant challenge. For proteins resistant to the traditional approach of directly crystallizing from detergents, lipidic phase crystallization can be a powerful tool. Bicelles are an excellent medium for crystallizing membrane proteins in a lipidic
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Presenilins are polytopic, integral proteins that control intramembranous proteolysis at the "gamma-" and "epsilon-" cleavage sites of the Alzheimer amyloid-beta precursor protein (APP) to yield amyloid-beta peptide (Abeta) and the APP intracellular domain (AICD). We have overexpressed a constitutively active
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Wild-type and mutant forms of bacteriorhodopsin (sbR) from Halobacterium salinarium, produced by Escherichia coli overexpression of a synthetic gene, were reversibly unfolded in 1, 2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 3-[(3-cholamidopropyl)dimethylamino]-2-hydroxyl-1-propane (CHAPSO), and sodium dodecyl sulfate (SDS) mixed micelles. To study the effect on
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